Johannes Buchner, Prof. - Publications

Chemistry Department Technical University Munich 
Chaperones, protein aggregation,protein folding

113 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Hoseini H, Pandey S, Jores T, Schmitt A, Franz-Wachtel M, Macek B, Buchner J, Dimmer KS, Rapaport D. The cytosolic co-chaperone Sti1 is relevant for mitochondrial biogenesis and morphology. The Febs Journal. PMID 27412066 DOI: 10.1111/febs.13813  0.96
2016 Schneider M, Rosam M, Glaser M, Patronov A, Shah H, Back KC, Daake MA, Buchner J, Antes I. BiPPred: Combined sequence- and structure-based prediction of peptide binding to the Hsp70 chaperone BiP. Proteins. PMID 27287023 DOI: 10.1002/prot.25084  0.96
2016 Nokwe CN, Hora M, Zacharias M, Yagi H, Peschek J, Reif B, Goto Y, Buchner J. Specific non-native interactions. Journal of Molecular Biology. PMID 26827727 DOI: 10.1016/j.jmb.2016.01.015  0.96
2016 Jahn M, Buchner J, Hugel T, Rief M. Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments. Proceedings of the National Academy of Sciences of the United States of America. PMID 26787848 DOI: 10.1073/pnas.1518827113  0.96
2015 Dashivets T, Thomann M, Rueger P, Knaupp A, Buchner J, Schlothauer T. Multi-Angle Effector Function Analysis of Human Monoclonal IgG Glycovariants. Plos One. 10: e0143520. PMID 26657484 DOI: 10.1371/journal.pone.0143520  0.96
2015 Mainz A, Peschek J, Stavropoulou M, Back KC, Bardiaux B, Asami S, Prade E, Peters C, Weinkauf S, Buchner J, Reif B. The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client. Nature Structural & Molecular Biology. PMID 26458046 DOI: 10.1038/nsmb.3108  0.96
2015 Nokwe CN, Hora M, Zacharias M, Yagi H, John C, Reif B, Goto Y, Buchner J. The Antibody Light-Chain Linker Is Important for Domain Stability and Amyloid Formation. Journal of Molecular Biology. 427: 3572-86. PMID 26408269 DOI: 10.1016/j.jmb.2015.09.012  0.96
2015 Ostankovitch M, Buchner J. The network of molecular chaperones: insights in the cellular proteostasis machinery. Journal of Molecular Biology. 427: 2899-903. PMID 26363891 DOI: 10.1016/j.jmb.2015.08.010  0.96
2015 Boczek EE, Reefschläger LG, Dehling M, Struller TJ, Häusler E, Seidl A, Kaila VR, Buchner J. Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90. Proceedings of the National Academy of Sciences of the United States of America. 112: E3189-98. PMID 26056257 DOI: 10.1073/pnas.1424342112  0.96
2015 Fleckenstein T, Kastenmüller A, Stein ML, Peters C, Daake M, Krause M, Weinfurtner D, Haslbeck M, Weinkauf S, Groll M, Buchner J. The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational Changes. Molecular Cell. 58: 1067-78. PMID 26009280 DOI: 10.1016/j.molcel.2015.04.019  0.96
2015 Röhl A, Wengler D, Madl T, Lagleder S, Tippel F, Herrmann M, Hendrix J, Richter K, Hack G, Schmid AB, Kessler H, Lamb DC, Buchner J. Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules. Nature Communications. 6: 6655. PMID 25851214 DOI: 10.1038/ncomms7655  0.96
2015 Haslbeck M, Buchner J. Assays to characterize molecular chaperone function in vitro. Methods in Molecular Biology (Clifton, N.J.). 1292: 39-51. PMID 25804746 DOI: 10.1007/978-1-4939-2522-3_3  0.96
2015 Huang B, Lucas T, Kueppers C, Dong X, Krause M, Bepperling A, Buchner J, Voshol H, Weiss A, Gerrits B, Kochanek S. Scalable production in human cells and biochemical characterization of full-length normal and mutant huntingtin. Plos One. 10: e0121055. PMID 25799558 DOI: 10.1371/journal.pone.0121055  0.96
2015 Röhl A, Tippel F, Bender E, Schmid AB, Richter K, Madl T, Buchner J. Hop/Sti1 phosphorylation inhibits its co-chaperone function. Embo Reports. 16: 240-9. PMID 25504578 DOI: 10.15252/embr.201439198  0.96
2015 Rehn AB, Buchner J. p23 and Aha1. Sub-Cellular Biochemistry. 78: 113-31. PMID 25487019 DOI: 10.1007/978-3-319-11731-7_6  0.96
2015 Haslbeck M, Peschek J, Buchner J, Weinkauf S. Structure and function of α-crystallins: Traversing from in vitro to in vivo Biochimica Et Biophysica Acta - General Subjects. DOI: 10.1016/j.bbagen.2015.06.008  0.96
2014 Jahn M, Rehn A, Pelz B, Hellenkamp B, Richter K, Rief M, Buchner J, Hugel T. The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function. Proceedings of the National Academy of Sciences of the United States of America. 111: 17881-6. PMID 25468961 DOI: 10.1073/pnas.1414073111  0.96
2014 Alvira S, Cuéllar J, Röhl A, Yamamoto S, Itoh H, Alfonso C, Rivas G, Buchner J, Valpuesta JM. Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop. Nature Communications. 5: 5484. PMID 25407331 DOI: 10.1038/ncomms6484  0.96
2014 Girstmair H, Buchner J. GET two for one. Molecular Cell. 56: 1-2. PMID 25280098 DOI: 10.1016/j.molcel.2014.09.015  0.96
2014 Zierer BK, Weiwad M, Rübbelke M, Freiburger L, Fischer G, Lorenz OR, Sattler M, Richter K, Buchner J. Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions. Angewandte Chemie (International Ed. in English). 53: 12257-62. PMID 25244159 DOI: 10.1002/anie.201406578  0.96
2014 Nokwe CN, Zacharias M, Yagi H, Hora M, Reif B, Goto Y, Buchner J. A residue-specific shift in stability and amyloidogenicity of antibody variable domains. The Journal of Biological Chemistry. 289: 26829-46. PMID 25096580 DOI: 10.1074/jbc.M114.582247  0.96
2014 Buchner J, Kessler H. Protein folding by interaction. Structure (London, England : 1993). 22: 936-7. PMID 25007223 DOI: 10.1016/j.str.2014.06.006  0.96
2014 Feige MJ, Buchner J. Principles and engineering of antibody folding and assembly. Biochimica Et Biophysica Acta. 1844: 2024-2031. PMID 24931831 DOI: 10.1016/j.bbapap.2014.06.004  0.96
2014 Feige MJ, Gräwert MA, Marcinowski M, Hennig J, Behnke J, Ausländer D, Herold EM, Peschek J, Castro CD, Flajnik M, Hendershot LM, Sattler M, Groll M, Buchner J. The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins. Proceedings of the National Academy of Sciences of the United States of America. 111: 8155-60. PMID 24830426 DOI: 10.1073/pnas.1321502111  0.96
2014 Paul A, Garcia YA, Zierer B, Patwardhan C, Gutierrez O, Hildenbrand Z, Harris DC, Balsiger HA, Sivils JC, Johnson JL, Buchner J, Chadli A, Cox MB. The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors. The Journal of Biological Chemistry. 289: 15297-308. PMID 24753260 DOI: 10.1074/jbc.M113.535229  0.96
2014 Lorenz OR, Freiburger L, Rutz DA, Krause M, Zierer BK, Alvira S, Cuéllar J, Valpuesta JM, Madl T, Sattler M, Buchner J. Modulation of the Hsp90 chaperone cycle by a stringent client protein. Molecular Cell. 53: 941-53. PMID 24613341 DOI: 10.1016/j.molcel.2014.02.003  0.96
2013 Kayser J, Haslbeck M, Dempfle L, Krause M, Grashoff C, Buchner J, Herrmann H, Bausch AR. The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks. Biophysical Journal. 105: 1778-85. PMID 24138853 DOI: 10.1016/j.bpj.2013.09.007  0.96
2013 Peschek J, Braun N, Rohrberg J, Back KC, Kriehuber T, Kastenmüller A, Weinkauf S, Buchner J. Regulated structural transitions unleash the chaperone activity of αB-crystallin. Proceedings of the National Academy of Sciences of the United States of America. 110: E3780-9. PMID 24043785 DOI: 10.1073/pnas.1308898110  0.96
2013 Bertz M, Buchner J, Rief M. Mechanical stability of the antibody domain CH3 homodimer in different oxidation states. Journal of the American Chemical Society. 135: 15085-91. PMID 24015948 DOI: 10.1021/ja405076j  0.96
2013 Beebe K, Mollapour M, Scroggins B, Prodromou C, Xu W, Tokita M, Taldone T, Pullen L, Zierer BK, Lee MJ, Trepel J, Buchner J, Bolon D, Chiosis G, Neckers L. Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors. Oncotarget. 4: 1065-74. PMID 23867252 DOI: 10.18632/oncotarget.1099  0.96
2013 Li J, Buchner J. Structure, function and regulation of the hsp90 machinery. Biomedical Journal. 36: 106-17. PMID 23806880 DOI: 10.4103/2319-4170.113230  0.96
2013 Hendershot LM, Feige MJ, Buchner J. Acidification activates ERp44--a molecular litmus test for protein assembly. Molecular Cell. 50: 779-81. PMID 23806332 DOI: 10.1016/j.molcel.2013.06.008  0.96
2013 Müller R, Gräwert MA, Kern T, Madl T, Peschek J, Sattler M, Groll M, Buchner J. High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation. Proceedings of the National Academy of Sciences of the United States of America. 110: 10183-8. PMID 23733956 DOI: 10.1073/pnas.1300547110  0.96
2013 Röhl A, Rohrberg J, Buchner J. The chaperone Hsp90: changing partners for demanding clients. Trends in Biochemical Sciences. 38: 253-62. PMID 23507089 DOI: 10.1016/j.tibs.2013.02.003  0.96
2013 Li J, Zoldak G, Kriehuber T, Soroka J, Schmid FX, Richter K, Buchner J. Unique proline-rich domain regulates the chaperone function of AIPL1. Biochemistry. 52: 2089-96. PMID 23418749 DOI: 10.1021/bi301648q  0.96
2013 Li J, Richter K, Reinstein J, Buchner J. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nature Structural & Molecular Biology. 20: 326-31. PMID 23396352 DOI: 10.1038/nsmb.2502  0.96
2013 Kateb F, Perrin H, Tripsianes K, Zou P, Spadaccini R, Bottomley M, Franzmann TM, Buchner J, Ansieau S, Sattler M. Structural and functional analysis of the DEAF-1 and BS69 MYND domains. Plos One. 8: e54715. PMID 23372760 DOI: 10.1371/journal.pone.0054715  0.96
2013 Marcinowski M, Rosam M, Seitz C, Elferich J, Behnke J, Bello C, Feige MJ, Becker CF, Antes I, Buchner J. Conformational selection in substrate recognition by Hsp70 chaperones. Journal of Molecular Biology. 425: 466-74. PMID 23207294 DOI: 10.1016/j.jmb.2012.11.030  0.96
2013 Retzlaff M, Rohrberg J, Küpper NJ, Lagleder S, Bepperling A, Manzenrieder F, Peschek J, Kessler H, Buchner J. The regulatory domain stabilizes the p53 tetramer by intersubunit contacts with the DNA binding domain. Journal of Molecular Biology. 425: 144-55. PMID 23103206 DOI: 10.1016/j.jmb.2012.10.015  0.96
2012 Bepperling A, Alte F, Kriehuber T, Braun N, Weinkauf S, Groll M, Haslbeck M, Buchner J. Alternative bacterial two-component small heat shock protein systems. Proceedings of the National Academy of Sciences of the United States of America. 109: 20407-12. PMID 23184973 DOI: 10.1073/pnas.1209565109  0.96
2012 Soroka J, Buchner J. Mechanistic aspects of the Hsp90 phosphoregulation. Cell Cycle (Georgetown, Tex.). 11: 1870-1. PMID 22544316 DOI: 10.4161/cc.20418  0.96
2012 Schreiber TB, Mäusbacher N, Soroka J, Wandinger SK, Buchner J, Daub H. Global analysis of phosphoproteome regulation by the Ser/Thr phosphatase Ppt1 in Saccharomyces cerevisiae. Journal of Proteome Research. 11: 2397-408. PMID 22369663 DOI: 10.1021/pr201134p  0.96
2012 Soroka J, Wandinger SK, Mäusbacher N, Schreiber T, Richter K, Daub H, Buchner J. Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. Molecular Cell. 45: 517-28. PMID 22365831 DOI: 10.1016/j.molcel.2011.12.031  0.96
2012 Schmid AB, Lagleder S, Gräwert MA, Röhl A, Hagn F, Wandinger SK, Cox MB, Demmer O, Richter K, Groll M, Kessler H, Buchner J. The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. The Embo Journal. 31: 1506-17. PMID 22227520 DOI: 10.1038/emboj.2011.472  0.96
2012 Li J, Soroka J, Buchner J. The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones. Biochimica Et Biophysica Acta. 1823: 624-35. PMID 21951723 DOI: 10.1016/j.bbamcr.2011.09.003  0.96
2012 Horwich AL, Buchner J, Smock RG, Gierasch LM, Saibil HR. Chaperones and protein folding Comprehensive Biophysics. 3: 212-237. DOI: 10.1016/B978-0-12-374920-8.00313-1  0.96
2011 Braun N, Zacharias M, Peschek J, Kastenmüller A, Zou J, Hanzlik M, Haslbeck M, Rappsilber J, Buchner J, Weinkauf S. Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach. Proceedings of the National Academy of Sciences of the United States of America. 108: 20491-6. PMID 22143763 DOI: 10.1073/pnas.1111014108  0.96
2011 Hagn F, Lagleder S, Retzlaff M, Rohrberg J, Demmer O, Richter K, Buchner J, Kessler H. Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53. Nature Structural & Molecular Biology. 18: 1086-93. PMID 21892170 DOI: 10.1038/nsmb.2114  0.96
2011 Kaiser E, Kroll C, Ernst K, Schwan C, Popoff M, Fischer G, Buchner J, Aktories K, Barth H. Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90. Infection and Immunity. 79: 3913-21. PMID 21768281 DOI: 10.1128/IAI.05372-11  0.96
2011 Richter K, Buchner J. Closing in on the Hsp90 chaperone-client relationship. Structure (London, England : 1993). 19: 445-6. PMID 21481768 DOI: 10.1016/j.str.2011.03.007  0.96
2011 Schroeder BO, Wu Z, Nuding S, Groscurth S, Marcinowski M, Beisner J, Buchner J, Schaller M, Stange EF, Wehkamp J. Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1. Nature. 469: 419-23. PMID 21248850 DOI: 10.1038/nature09674  0.96
2011 Marcinowski M, Höller M, Feige MJ, Baerend D, Lamb DC, Buchner J. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nature Structural & Molecular Biology. 18: 150-8. PMID 21217698 DOI: 10.1038/nsmb.1970  0.96
2011 Li J, Richter K, Buchner J. Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nature Structural & Molecular Biology. 18: 61-6. PMID 21170051 DOI: 10.1038/nsmb.1965  0.96
2011 Dmochewitz L, Lillich M, Kaiser E, Jennings LD, Lang AE, Buchner J, Fischer G, Aktories K, Collier RJ, Barth H. Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen. Cellular Microbiology. 13: 359-73. PMID 20946244 DOI: 10.1111/j.1462-5822.2010.01539.x  0.96
2010 Richter K, Haslbeck M, Buchner J. The heat shock response: life on the verge of death. Molecular Cell. 40: 253-66. PMID 20965420 DOI: 10.1016/j.molcel.2010.10.006  0.96
2010 Anselment B, Baerend D, Mey E, Buchner J, Weuster-Botz D, Haslbeck M. Experimental optimization of protein refolding with a genetic algorithm. Protein Science : a Publication of the Protein Society. 19: 2085-95. PMID 20799347 DOI: 10.1002/pro.488  0.96
2010 Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Molecular Cell. 39: 507-20. PMID 20797624 DOI: 10.1016/j.molcel.2010.08.001  0.96
2010 Ratzke C, Mickler M, Hellenkamp B, Buchner J, Hugel T. Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle. Proceedings of the National Academy of Sciences of the United States of America. 107: 16101-6. PMID 20736353 DOI: 10.1073/pnas.1000916107  0.96
2010 Bertz M, Chen J, Feige MJ, Franzmann TM, Buchner J, Rief M. Structural and mechanical hierarchies in the alpha-crystallin domain dimer of the hyperthermophilic small heat shock protein Hsp16.5. Journal of Molecular Biology. 400: 1046-56. PMID 20595041 DOI: 10.1016/j.jmb.2010.05.065  0.96
2010 Kriehuber T, Rattei T, Weinmaier T, Bepperling A, Haslbeck M, Buchner J. Independent evolution of the core domain and its flanking sequences in small heat shock proteins. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 24: 3633-42. PMID 20501794 DOI: 10.1096/fj.10-156992  0.96
2010 Feige MJ, Simpson ER, Herold EM, Bepperling A, Heger K, Buchner J. Dissecting the alternatively folded state of the antibody Fab fragment. Journal of Molecular Biology. 399: 719-30. PMID 20434459 DOI: 10.1016/j.jmb.2010.04.032  0.96
2010 Rudolph B, Gebendorfer KM, Buchner J, Winter J. Evolution of Escherichia coli for growth at high temperatures. The Journal of Biological Chemistry. 285: 19029-34. PMID 20406805 DOI: 10.1074/jbc.M110.103374  0.96
2010 Echeverria PC, Figueras MJ, Vogler M, Kriehuber T, de Miguel N, Deng B, Dalmasso MC, Matthews DE, Matrajt M, Haslbeck M, Buchner J, Angel SO. The Hsp90 co-chaperone p23 of Toxoplasma gondii: Identification, functional analysis and dynamic interactome determination. Molecular and Biochemical Parasitology. 172: 129-40. PMID 20403389 DOI: 10.1016/j.molbiopara.2010.04.004  0.96
2010 Buchner J. Bacterial Hsp90--desperately seeking clients. Molecular Microbiology. 76: 540-4. PMID 20345652 DOI: 10.1111/j.1365-2958.2010.07140.x  0.96
2010 Chen J, Feige MJ, Franzmann TM, Bepperling A, Buchner J. Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization. Journal of Molecular Biology. 398: 122-31. PMID 20171228 DOI: 10.1016/j.jmb.2010.02.022  0.96
2010 Retzlaff M, Hagn F, Mitschke L, Hessling M, Gugel F, Kessler H, Richter K, Buchner J. Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Molecular Cell. 37: 344-54. PMID 20159554 DOI: 10.1016/j.molcel.2010.01.006  0.96
2010 Jinwal UK, Koren J, Borysov SI, Schmid AB, Abisambra JF, Blair LJ, Johnson AG, Jones JR, Shults CL, O'Leary JC, Jin Y, Buchner J, Cox MB, Dickey CA. The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 30: 591-9. PMID 20071522 DOI: 10.1523/JNEUROSCI.4815-09.2010  0.96
2010 Feige MJ, Hendershot LM, Buchner J. How antibodies fold. Trends in Biochemical Sciences. 35: 189-98. PMID 20022755 DOI: 10.1016/j.tibs.2009.11.005  0.96
2010 Feige MJ, Hendershot LM, Buchner J. Response to Corcos: exceptions to the rules Trends in Biochemical Sciences. 35: 594. DOI: 10.1016/j.tibs.2010.07.011  0.96
2009 Tsutsumi S, Mollapour M, Graf C, Lee CT, Scroggins BT, Xu W, Haslerova L, Hessling M, Konstantinova AA, Trepel JB, Panaretou B, Buchner J, Mayer MP, Prodromou C, Neckers L. Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nature Structural & Molecular Biology. 16: 1141-7. PMID 19838189 DOI: 10.1038/nsmb.1682  0.96
2009 Müller M, Richter K, Heuck A, Kremmer E, Buchner J, Jansen RP, Niessing D. Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization. Rna (New York, N.Y.). 15: 2002-12. PMID 19710186 DOI: 10.1261/rna.1753309  0.96
2009 de Miguel N, Braun N, Bepperling A, Kriehuber T, Kastenmüller A, Buchner J, Angel SO, Haslbeck M. Structural and functional diversity in the family of small heat shock proteins from the parasite Toxoplasma gondii. Biochimica Et Biophysica Acta. 1793: 1738-48. PMID 19699241 DOI: 10.1016/j.bbamcr.2009.08.005  0.96
2009 Retzlaff M, Stahl M, Eberl HC, Lagleder S, Beck J, Kessler H, Buchner J. Hsp90 is regulated by a switch point in the C-terminal domain. Embo Reports. 10: 1147-53. PMID 19696785 DOI: 10.1038/embor.2009.153  0.96
2009 Peschek J, Braun N, Franzmann TM, Georgalis Y, Haslbeck M, Weinkauf S, Buchner J. The eye lens chaperone alpha-crystallin forms defined globular assemblies. Proceedings of the National Academy of Sciences of the United States of America. 106: 13272-7. PMID 19651604 DOI: 10.1073/pnas.0902651106  0.96
2009 Simpson ER, Herold EM, Buchner J. The folding pathway of the antibody V(L) domain. Journal of Molecular Biology. 392: 1326-38. PMID 19647749 DOI: 10.1016/j.jmb.2009.07.075  0.96
2009 Feige MJ, Nath S, Catharino SR, Weinfurtner D, Steinbacher S, Buchner J. Structure of the murine unglycosylated IgG1 Fc fragment. Journal of Molecular Biology. 391: 599-608. PMID 19559712 DOI: 10.1016/j.jmb.2009.06.048  0.96
2009 Hainzl O, Lapina MC, Buchner J, Richter K. The charged linker region is an important regulator of Hsp90 function. The Journal of Biological Chemistry. 284: 22559-67. PMID 19553666 DOI: 10.1074/jbc.M109.031658  0.96
2009 Feige MJ, Groscurth S, Marcinowski M, Shimizu Y, Kessler H, Hendershot LM, Buchner J. An unfolded CH1 domain controls the assembly and secretion of IgG antibodies. Molecular Cell. 34: 569-79. PMID 19524537 DOI: 10.1016/j.molcel.2009.04.028  0.96
2009 Dashivets T, Wood N, Hergersberg C, Buchner J, Haslbeck M. Rapid matrix-assisted refolding of histidine-tagged proteins. Chembiochem : a European Journal of Chemical Biology. 10: 869-76. PMID 19235820 DOI: 10.1002/cbic.200800697  0.96
2009 Mickler M, Hessling M, Ratzke C, Buchner J, Hugel T. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Nature Structural & Molecular Biology. 16: 281-6. PMID 19234469 DOI: 10.1038/nsmb.1557  0.96
2009 Hessling M, Richter K, Buchner J. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nature Structural & Molecular Biology. 16: 287-93. PMID 19234467 DOI: 10.1038/nsmb.1565  0.96
2009 Pandya MJ, Bendz H, Manzenrieder F, Noessner E, Kessler H, Buchner J, Issels RD. Interaction of human heat shock protein 70 with tumor-associated peptides. Biological Chemistry. 390: 305-12. PMID 19199830 DOI: 10.1515/BC.2009.038  0.96
2009 Altmann KH, Buchner J, Kessler H, Diederich F, Kräutler B, Lippard S, Liskamp R, Müller K, Nolan EM, Samori B, Schneider G, Schreiber SL, Schwalbe H, Toniolo C, van Boeckel CA, et al. The state of the art of chemical biology. Chembiochem : a European Journal of Chemical Biology. 10: 16-29. PMID 19115274 DOI: 10.1002/cbic.200800758  0.96
2008 Feige MJ, Groscurth S, Marcinowski M, Yew ZT, Truffault V, Paci E, Kessler H, Buchner J. The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity. Proceedings of the National Academy of Sciences of the United States of America. 105: 13373-8. PMID 18768806 DOI: 10.1073/pnas.0802809105  0.96
2008 Schmid K, Haslbeck M, Buchner J, Somoza V. Induction of heat shock proteins and the proteasome system by casein-N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)lysine in Caco-2 cells. Annals of the New York Academy of Sciences. 1126: 257-61. PMID 18448826 DOI: 10.1196/annals.1433.062  0.96
2008 Wandinger SK, Richter K, Buchner J. The Hsp90 chaperone machinery. The Journal of Biological Chemistry. 283: 18473-7. PMID 18442971 DOI: 10.1074/jbc.R800007200  0.96
2008 Richter K, Soroka J, Skalniak L, Leskovar A, Hessling M, Reinstein J, Buchner J. Conserved conformational changes in the ATPase cycle of human Hsp90. The Journal of Biological Chemistry. 283: 17757-65. PMID 18400751 DOI: 10.1074/jbc.M800540200  0.96
2008 Haslbeck M, Kastenmüller A, Buchner J, Weinkauf S, Braun N. Structural dynamics of archaeal small heat shock proteins. Journal of Molecular Biology. 378: 362-74. PMID 18353362 DOI: 10.1016/j.jmb.2008.01.095  0.96
2008 Leskovar A, Wegele H, Werbeck ND, Buchner J, Reinstein J. The ATPase cycle of the mitochondrial Hsp90 analog Trap1. The Journal of Biological Chemistry. 283: 11677-88. PMID 18287101 DOI: 10.1074/jbc.M709516200  0.96
2008 Franzmann TM, Menhorn P, Walter S, Buchner J. Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain. Molecular Cell. 29: 207-16. PMID 18243115 DOI: 10.1016/j.molcel.2007.11.025  0.96
2008 Frey S, Haslbeck M, Hainzl O, Buchner J. Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system. Biological Chemistry. 389: 37-45. PMID 18095868 DOI: 10.1515/BC.2008.007  0.96
2008 Richter K, Meinlschmidt B, Buchner J. Hsp90: From Dispensable Heat Shock Protein to Global Player Protein Folding Handbook. 2: 768-829. DOI: 10.1002/9783527619498.ch56  0.96
2008 Buchner J, Walter S. Analysis of Chaperone Function in Vitro Protein Folding Handbook. 1: 162-196. DOI: 10.1002/9783527619498.ch38  0.96
2008 Buchner J, Kiefhaber T. Protein Folding Handbook Protein Folding Handbook. 1: 1-1333. DOI: 10.1002/9783527619498  0.96
2007 Heuck A, Du TG, Jellbauer S, Richter K, Kruse C, Jaklin S, Müller M, Buchner J, Jansen RP, Niessing D. Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes. Proceedings of the National Academy of Sciences of the United States of America. 104: 19778-83. PMID 18056806 DOI: 10.1073/pnas.0706780104  0.96
2007 Richter K, Reinstein J, Buchner J. A Grp on the Hsp90 mechanism. Molecular Cell. 28: 177-9. PMID 17964255 DOI: 10.1016/j.molcel.2007.10.007  0.96
2007 Riggs DL, Cox MB, Tardif HL, Hessling M, Buchner J, Smith DF. Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling. Molecular and Cellular Biology. 27: 8658-69. PMID 17938211 DOI: 10.1128/MCB.00985-07  0.96
2007 Frey S, Leskovar A, Reinstein J, Buchner J. The ATPase cycle of the endoplasmic chaperone Grp94. The Journal of Biological Chemistry. 282: 35612-20. PMID 17925398 DOI: 10.1074/jbc.M704647200  0.96
2007 Janig E, Haslbeck M, Aigelsreiter A, Braun N, Unterthor D, Wolf P, Khaskhely NM, Buchner J, Denk H, Zatloukal K. Clusterin associates with altered elastic fibers in human photoaged skin and prevents elastin from ultraviolet-induced aggregation in vitro. The American Journal of Pathology. 171: 1474-82. PMID 17872975 DOI: 10.2353/ajpath.2007.061064  0.96
2007 Cox MB, Riggs DL, Hessling M, Schumacher F, Buchner J, Smith DF. FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity. Molecular Endocrinology (Baltimore, Md.). 21: 2956-67. PMID 17717070 DOI: 10.1210/me.2006-0547  0.96
2007 Bendz H, Ruhland SC, Pandya MJ, Hainzl O, Riegelsberger S, Braüchle C, Mayer MP, Buchner J, Issels RD, Noessner E. Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling. The Journal of Biological Chemistry. 282: 31688-702. PMID 17684010 DOI: 10.1074/jbc.M704129200  0.96
2007 Feige MJ, Hagn F, Esser J, Kessler H, Buchner J. Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain. Journal of Molecular Biology. 365: 1232-44. PMID 17112539 DOI: 10.1016/j.jmb.2006.10.049  0.96
2006 Scheibel T, Buchner J. Protein aggregation as a cause for disease. Handbook of Experimental Pharmacology. 199-219. PMID 16610361  0.56
2005 Shaner L, Wegele H, Buchner J, Morano KA. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb. The Journal of Biological Chemistry. 280: 41262-9. PMID 16221677 DOI: 10.1074/jbc.M503614200  0.96
2005 Catharino S, Buchner J, Walter S. Characterization of oligomeric species in the fibrillization pathway of the yeast prion Ure2p. Biological Chemistry. 386: 633-41. PMID 16207084 DOI: 10.1515/BC.2005.074  0.96
2004 Vinci F, Catharino S, Frey S, Buchner J, Marino G, Pucci P, Ruoppolo M. Hierarchical formation of disulfide bonds in the immunoglobulin Fc fragment is assisted by protein-disulfide isomerase. The Journal of Biological Chemistry. 279: 15059-66. PMID 14729662 DOI: 10.1074/jbc.M311480200  0.96
1999 Scheibel T, Siegmund HI, Jaenicke R, Ganz P, Lilie H, Buchner J. The charged region of Hsp90 modulates the function of the N-terminal domain. Proceedings of the National Academy of Sciences of the United States of America. 96: 1297-302. PMID 9990018 DOI: 10.1073/pnas.96.4.1297  0.96
1998 Nichtl A, Buchner J, Jaenicke R, Rudolph R, Scheibel T. Folding and association of beta-Galactosidase. Journal of Molecular Biology. 282: 1083-91. PMID 9753555 DOI: 10.1006/jmbi.1998.2075  0.96
1995 Lilie H, Jaenicke R, Buchner J. Characterization of a quaternary-structured folding intermediate of an antibody Fab-fragment. Protein Science : a Publication of the Protein Society. 4: 917-24. PMID 7663347 DOI: 10.1002/pro.5560040511  0.96
1994 Schmidt M, Rutkat K, Rachel R, Pfeifer G, Jaenicke R, Viitanen P, Lorimer G, Buchner J. Symmetric complexes of GroE chaperonins as part of the functional cycle. Science (New York, N.Y.). 265: 656-9. PMID 7913554 DOI: 10.1126/science.7913554  0.96
1992 Kern G, Schmidt M, Buchner J, Jaenicke R. Glycosylation inhibits the interaction of invertase with the chaperone GroEL. Febs Letters. 305: 203-5. PMID 1363729  0.8
1991 Buchner J, Renner M, Lilie H, Hinz HJ, Jaenicke R, Kiefhabel T, Rudolph R. Alternatively folded states of an immunoglobulin. Biochemistry. 30: 6922-9. PMID 1906346  0.8
1991 Buchner J, Schmidt M, Fuchs M, Jaenicke R, Rudolph R, Schmid FX, Kiefhaber T. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry. 30: 1586-91. PMID 1671555  0.96
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